Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States

Dan Y. Gui; Caroline A. Lewis; Matthew G. Vander Heiden

doi:10.1126/scisignal.2003925

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Abstract

Pyruvate kinase isoform M2 (PKM2) activity is subject to complex allosteric regulation. Recently, serine and SAICAR (succinylaminoimidazolecarboxamide ribose-5′-phosphate) were identified as previously unrecognized activators of PKM2. These findings add additional complexity to how PKM2 is regulated in cells and support the notion that modulating PKM2 activity enables cells to adapt their metabolic state to specific physiological contexts.

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Sci. Signal.

Vol 6, Issue 263
19 February 2013

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Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States

By Dan Y. Gui, Caroline A. Lewis, Matthew G. Vander Heiden

Sci. Signal.19 Feb 2013 : pe7

Regulation of the metabolic enzyme PKM2 enables cells to switch from a growth-promoting to an energy-producing state.

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Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States

By Dan Y. Gui, Caroline A. Lewis, Matthew G. Vander Heiden

Sci. Signal.19 Feb 2013 : pe7

Regulation of the metabolic enzyme PKM2 enables cells to switch from a growth-promoting to an energy-producing state.

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